Header list of 1r4h.pdb file
Complete list - 2 202 Bytes
HEADER RNA 06-OCT-03 1R4H
TITLE NMR SOLUTION STRUCTURE OF THE IIIC DOMAIN OF GB VIRUS B IRES ELEMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-R(*GP*GP*GP*CP*AP*AP*GP*CP*CP*C)-3';
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE OCCURS NATURALLY IN GB VIRUS B AND WAS
SOURCE 4 SYNTHESIZED IN VITRO TRANCRIPTION USING T7 RNA POLYMERASE.
KEYWDS GB VIRUS B, IRES, HAIRPIN LOOP, RNA
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR K.KALUARACHCHI,V.THIVIYANATHAN,R.RIJINBRAND,S.M.LEMON,D.G.GORENSTEIN
REVDAT 4 02-MAR-22 1R4H 1 REMARK
REVDAT 3 24-FEB-09 1R4H 1 VERSN
REVDAT 2 15-FEB-05 1R4H 1 JRNL
REVDAT 1 19-OCT-04 1R4H 0
JRNL AUTH R.RIJNBRAND,V.THIVIYANATHAN,K.KALUARACHCHI,S.M.LEMON,
JRNL AUTH 2 D.G.GORENSTEIN
JRNL TITL MUTATIONAL AND STRUCTURAL ANALYSIS OF STEM-LOOP IIIC OF THE
JRNL TITL 2 HEPATITIS C VIRUS AND GB VIRUS B INTERNAL RIBOSOME ENTRY
JRNL TITL 3 SITES.
JRNL REF J.MOL.BIOL. V. 343 805 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15476802
JRNL DOI 10.1016/J.JMB.2004.08.095
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER, A
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020425.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 10 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM PHOSPHATE, 10 MM KCL, 0.05
REMARK 210 MM EDTA PH 6.8, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING RESTRAINED MOLECULAR
REMARK 210 DYNAMICS COMPLETE RELAXATION
REMARK 210 MATRIX
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H1' A A 5 H5' A A 6 1.12
REMARK 500 H41 C A 4 O6 G A 7 1.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES
REMARK 500 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES
REMARK 500 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.8 DEGREES
REMARK 500 A A 5 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 A A 6 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 G A 7 N7 - C8 - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 G A 7 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R4H A 1 10 PDB 1R4H 1R4H 1 10
SEQRES 1 A 10 G G G C A A G C C C
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 2 202 Bytes